The DOI matches its Crossref record; 5 of the 5 references it cites were found in a registry or an index.
Collagens, modifying enzymes and their mutations in humans, flies and worms
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
Lysyl oxidase: properties, specificity, and biological roles inside and outside of the cell
Kagan, H. M., & Li, W. (2003) · Journal of Cellular Biochemistry · doi:10.1002/jcb.10413 · Cited by 954
Characterization of the human prolyl 4-hydroxylases that modify the hypoxia-inducible factor
Hirsilä, M., Koivunen, P., Günzler, V., Kivirikko, K. I., & Myllyharju, J. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m304982200 · Cited by 794
Self-citationIvan, M., Haberberger, T., Gervasi, D. C., Michelson, K. S., Günzler, V., Kondo, K., Yang, H., Sorokina, I., Conaway, R. C., Conaway, J. W., et al. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.192342099 · Cited by 561
Edens, W. A., Sharling, L., Cheng, G., Shapira, R., Kinkade, J. M., Lee, T., Edens, H. A., Tang, X., Sullards, C., Flaherty, D. B., et al. (2001) · The Journal of Cell Biology · doi:10.1083/jcb.200103132 · Cited by 375
Steinmann, B., Royce, P. M., & Superti‐Furga, A. (2002) · Connective Tissue and Its Heritable Disorders · doi:10.1002/0471221929.ch9 · Cited by 358
Cited by
The extracellular matrix at a glance
Frantz, C., Stewart, K. M., & Weaver, V. M. (2010) · Journal of Cell Science · doi:10.1242/jcs.023820 · Cited by 4,334
Extracellular matrix structure
Theocharis, A. D., Skandalis, S. S., Gialeli, C., & Karamanos, N. K. (2016) · Advanced Drug Delivery Reviews · doi:10.1016/j.addr.2015.11.001 · Cited by 2,598
Ricard-Blum, S. (2011) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a004978 · Cited by 2,305
Concepts of extracellular matrix remodelling in tumour progression and metastasis
Winkler, J., Abisoye-Ogunniyan, A., Metcalf, K. J., & Werb, Z. (2020) · Nature Communications · doi:10.1038/s41467-020-18794-x · Cited by 2,296
Hypoxia and the extracellular matrix: drivers of tumour metastasis
Gilkes, D. M., Semenza, G. L., & Wirtz, D. (2014) · Nature Reviews Cancer · doi:10.1038/nrc3726 · Cited by 1,520
Extracellular Matrix Assembly: A Multiscale Deconstruction
Mouw, J. K., Ou, G., & Weaver, V. M. (2014) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3902 · Cited by 1,534
Jabłońska-Trypuć, A., Matejczyk, M., & Rosochacki, S. (2016) · Journal of Enzyme Inhibition and Medicinal Chemistry · doi:10.3109/14756366.2016.1161620 · Cited by 1,042
The role of collagen in bone strength
Viguet-Carrin, S., Garnero, P., & Delmas, P. D. (2006) · Osteoporosis International · doi:10.1007/s00198-005-2035-9 · Cited by 1,047
Marini, J. C., Forlino, A., Bächinger, H. P., Bishop, N. J., Byers, P. H., Paepe, A. D., Fassier, F., Fratzl-Zelman, N., Kozloff, K. M., Krakow, D., et al. (2017) · Nature Reviews Disease Primers · doi:10.1038/nrdp.2017.52 · Cited by 842
Khoshnoodi, J., Pedchenko, V., & Hudson, B. G. (2008) · Microscopy Research and Technique · doi:10.1002/jemt.20564 · Cited by 668
Gorres, K. L., & Raines, R. T. (2010) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.3109/10409231003627991 · Cited by 591
Collagen as a double-edged sword in tumor progression
Fang, M., Yuan, J., Peng, C., & Li, Y. (2014) · Tumor Biology · doi:10.1007/s13277-013-1511-7 · Cited by 580
Processing of collagen based biomaterials and the resulting materials properties
Meyer, M. (2019) · BioMedical Engineering OnLine · doi:10.1186/s12938-019-0647-0 · Cited by 539
Inhibition of Hypoxia-inducible Factor (HIF) Hydroxylases by Citric Acid Cycle Intermediates
Koivunen, P., Hirsilä, M., Remes, A. M., Hassinen, I. E., Kivirikko, K. I., & Myllyharju, J. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m610415200 · Cited by 521
Self-citationOncogenic Isocitrate Dehydrogenase Mutations: Mechanisms, Models, and Clinical Opportunities
Cairns, R. A., & Mak, T. W. (2013) · Cancer Discovery · doi:10.1158/2159-8290.cd-13-0083 · Cited by 452
Vitamin C: Update on physiology and pharmacology
Mandl, J., Szarka, A., & Bánhegyi, G. (2009) · British Journal of Pharmacology · doi:10.1111/j.1476-5381.2009.00282.x · Cited by 451
The collagen family members as cell adhesion proteins
Heino, J. (2007) · BioEssays · doi:10.1002/bies.20636 · Cited by 439
The Ehlers–Danlos syndrome, a disorder with many faces
De Paepe, A., & Malfait, F. (2012) · Clinical Genetics · doi:10.1111/j.1399-0004.2012.01858.x · Cited by 379
Prediction of collagen stability from amino acid sequence
Persikov, A. V., Ramshaw, J. A. M., & Brodsky, B. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m501657200 · Cited by 349
Transmembrane collagen receptors
Leitinger, B. (2011) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev-cellbio-092910-154013 · Cited by 354
Genetic diseases of connective tissues: cellular and extracellular effects of ECM mutations
Bateman, J. F., Boot-Handford, R. P., & Lamandé, S. R. (2009) · Nature Reviews Genetics · doi:10.1038/nrg2520 · Cited by 338
Gliomedin mediates Schwann cell-axon interaction and the molecular assembly of the nodes of Ranvier
Eshed, Y., Feinberg, K., Poliak, S., Sabanay, H., Sarig-Nadir, O., Spiegel, I., Bermingham, J. R., & Peles, E. (2005) · Neuron · doi:10.1016/j.neuron.2005.06.026 · Cited by 321
Singh, B., Fleury, C., Jalalvand, F., & Riesbeck, K. (2012) · FEMS Microbiology Reviews · doi:10.1111/j.1574-6976.2012.00340.x · Cited by 302
RETRACTED: Collagen Prolyl Hydroxylases Are Essential for Breast Cancer Metastasis
Gilkes, D. M., Chaturvedi, P., Bajpai, S., Wong, C. C., Wei, H., Pitcairn, S., Hubbi, M. E., Wirtz, D., & Semenza, G. L. (2013) · Cancer Research · doi:10.1158/0008-5472.can-12-3963 · Cited by 296
RetractedSasaki, M., Knobbe, C. B., Itsumi, M., Elia, A. J., Harris, I. S., Chio, I. I. C., Cairns, R. A., McCracken, S., Wakeham, A., Haight, J., et al. (2012) · Genes & Development · doi:10.1101/gad.198200.112 · Cited by 296
Loenarz, C., & Schofield, C. J. (2011) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2010.07.002 · Cited by 274
Structural studies on human 2-oxoglutarate dependent oxygenases
McDonough, M. A., Loenarz, C., Chowdhury, R., Clifton, I. J., & Schofield, C. J. (2010) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2010.08.006 · Cited by 280
Cockman, M. E., Lancaster, D. E., Stolze, I. P., Hewitson, K. S., McDonough, M. A., Coleman, M. L., Coles, C. H., Yu, X., Hay, R. T., Ley, S. C., et al. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0606877103 · Cited by 285
Role of hypoxia-inducible factors in breast cancer metastasis
Gilkes, D. M., & Semenza, G. L. (2013) · Future Oncology · doi:10.2217/fon.13.92 · Cited by 274
Procollagen lysyl hydroxylase 2 is essential for hypoxia-induced breast cancer metastasis
Gilkes, D. M., Bajpai, S., Wong, C. C., Chaturvedi, P., Hubbi, M. E., Wirtz, D., & Semenza, G. L. (2013) · Molecular Cancer Research · doi:10.1158/1541-7786.mcr-12-0629 · Cited by 252
RetractedSkin collagen through the lifestages: importance for skin health and beauty
Reilly, D. M., & Lozano, J. (2021) · Plastic and Aesthetic Research · doi:10.20517/2347-9264.2020.153 · Cited by 241
Cell-matrix interactions in dermal repair and scarring
Eckes, B., Nischt, R., & Krieg, T. (2010) · Fibrogenesis & Tissue Repair · doi:10.1186/1755-1536-3-4 · Cited by 205
The HIF pathway and erythrocytosis
Lee, F. S., & Percy, M. J. (2011) · Annual Review of Pathology Mechanisms of Disease · doi:10.1146/annurev-pathol-011110-130321 · Cited by 177
Molecular insights into prolyl and lysyl hydroxylation of fibrillar collagens in health and disease
Gjaltema, R. A. F., & Bank, R. A. (2017) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.1080/10409238.2016.1269716 · Cited by 175
Matrix molecules and skin biology
Nyström, A., & Bruckner-Tuderman, L. (2019) · Seminars in Cell & Developmental Biology · doi:10.1016/j.semcdb.2018.07.025 · Cited by 144
Collagen Remodeling in the Hypoxic Tumor-Mesothelial Niche Promotes Ovarian Cancer Metastasis
Natarajan, S., Foreman, K. M., Soriano, M. I., Rossen, N. S., Shehade, H., Fregoso, D. R., Eggold, J. T., Krishnan, V., Dorigo, O., Krieg, A. J., et al. (2019) · Cancer Research · doi:10.1158/0008-5472.can-18-2616 · Cited by 129
Bourgot, I., Primac, I., Louis, T., Noël, A., & Maquoi, E. (2020) · Frontiers in Oncology · doi:10.3389/fonc.2020.01488 · Cited by 113
Shi, J., Son, M.-Y., Yamada, S., Szabova, L., Kahan, S., Chrysovergis, K., Wolf, L., Surmak, A., & Holmbeck, K. (2008) · Developmental Biology · doi:10.1016/j.ydbio.2007.10.017 · Cited by 107
Secreted gliomedin is a perinodal matrix component of peripheral nerves
Eshed, Y., Feinberg, K., Carey, D. J., & Peles, E. (2007) · The Journal of Cell Biology · doi:10.1083/jcb.200612139 · Cited by 103
Molecular pathways of cell-mediated degradation of fibrillar collagen
Sprangers, S., & Everts, V. (2019) · Matrix Biology · doi:10.1016/j.matbio.2017.11.008 · Cited by 102
Chiarelli, N., Ritelli, M., Zoppi, N., & Colombi, M. (2019) · Genes · doi:10.3390/genes10080609 · Cited by 82
Collagen Prolyl 4-Hydroxylase as a Therapeutic Target: Miniperspective
Vasta, J. D., & Raines, R. T. (2018) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.8b00822 · Cited by 82
Zhao, T., Chen, H., Cheng, C., Zhang, J., Yan, Z., Kuang, J., Kong, F., Li, C., & Lu, Q. (2019) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2019.109224 · Cited by 52
Heikkinen, A., Pihlajaniemi, T., Faissner, A., & Yuzaki, M. (2014) · Progress in Brain Research · doi:10.1016/b978-0-444-63486-3.00002-5 · Cited by 42
Selective Inhibition of Collagen Prolyl 4-Hydroxylase in Human Cells
Vasta, J. D., Andersen, K. A., Deck, K. M., Nizzi, C. P., Eisenstein, R. S., & Raines, R. T. (2016) · ACS Chemical Biology · doi:10.1021/acschembio.5b00749 · Cited by 41
Selective inhibition of prolyl 4-hydroxylases by bipyridinedicarboxylates
Vasta, J. D., & Raines, R. T. (2015) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2015.05.003 · Cited by 16
Glimpses into the molecular pathogenesis of Peyronie’s disease
ten Dam, E.-J. P. M., van Driel, M. F., de Jong, I. J., Werker, P. M. N., & Bank, R. A. (2020) · The Aging Male · doi:10.1080/13685538.2019.1643311 · Cited by 15
“Conversion of proline into 3-hydroxyproline or 4hydroxyproline is catalyzed by prolyl hydroxylases, conversion of lysine (Lys) into 4-hydroxylysine (Hyl) by lysyl hydroxylases, and cross-linking is initiated by lysyl oxidases [47].”
Background
Metadata
- Authors
- Myllyharju, J.
- Venue
- Trends in Genetics
- Publisher
- Elsevier BV
- Published
- 2004-01
- Volume
- 20
- Issue
- 1
- Pages
- 33-43
- ISSN
- 0168-9525 (ISSN-L)
- OpenAlex
- W2003305541
- Cited by
- 1,180
- References
- 5
- FWCI
- 21.27
- Type
- journal article
- Language
- en
- Open access
- closed
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
Data sources
Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
